UL32_VZVD
ID UL32_VZVD Reviewed; 585 AA.
AC P09282;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Packaging protein UL32;
GN Name=26;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
CC -!- FUNCTION: Plays a role in efficient localization of neo-synthesized
CC capsids to nuclear replication compartments, thereby controlling
CC cleavage and packaging of virus genomic DNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm. Host nucleus. Note=Mainly
CC cytoplasmic in transfected cell culture. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae UL32 protein family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an envelope glycoprotein.
CC {ECO:0000305}.
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DR EMBL; X04370; CAA27908.1; -; Genomic_DNA.
DR PIR; H27343; WZBE26.
DR SMR; P09282; -.
DR PRIDE; P09282; -.
DR Proteomes; UP000002602; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR002597; Herpes_env.
DR Pfam; PF01673; Herpes_env; 1.
DR PROSITE; PS51988; HERPESVIRUS_UL32; 1.
PE 3: Inferred from homology;
KW Host cytoplasm; Host nucleus; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..585
FT /note="Packaging protein UL32"
FT /id="PRO_0000116019"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..193
FT /note="Zinc finger 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT REGION 408..491
FT /note="Zinc finger 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 491
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
SQ SEQUENCE 585 AA; 65695 MW; 8C7BB93E2A12FC15 CRC64;
MDRVESEEPM DGFESPVFSE NTSSNSGWCS DAFSDSYIAY NPALLLKNDL LFSELLFASH
LINVPRAIEN NVTYEASSAV GVDNEMTSST TEFIEEIGDV LALDRACLVC RTLDLYKRKF
GLTPEWVADY AMLCMKSLAS PPCAVVTFSA AFEFVYLMDR YYLCRYNVTL VGSFARRTLS
LLDIQRHFFL HVCFRTDGGL PGIRPPPGKE MANKVRYSNY SFFVQAVVRA ALLSISTSRL
DETETRKSFY FNQDGLTGGP QPLAAALANW KDCARMVDCS SSEHRTSGMI TCAERALKED
IEFEDILIDK LKKSSYVEAA WGYADLALLL LSGVATWNVD ERTNCAIETR VGCVKSYWQA
NRIENSRDVP KQFSKFTSED ACPEVAFGPI LLTTLKNAKC RGRTNTECML CCLLTIGHYW
IALRQFKRDI LAYSANNTSL FDCIEPVINA WSLDNPIKLK FPFNDEGRFI TIVKAAGSEA
VYKHLFCDLL CALSELQTNP KILFAHPTTA DKEVLELYKA QLAAQNRFEG RVCAGLWTLA
YAFKAYQIFP RKPTANAAFI RDGGLMLRRH AISLVSLEHT LSKYV